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Open Access Green as soon as Postprint is submitted to ZB.
Codeposition of Apolipoprotein A-IV and Transthyretin in Senile Systemic (ATTR) Amyloidosis.
Biochem. Biophys. Res. Commun. 285, 903-908 (2001)
Protein material was extracted from amyloid-rich sections of formalin-fixed and paraffin-embedded heart tissue from an individual with senile systemic amyloidosis, known to contain wild-type transthyretin as major amyloid fibril protein. Amino acid sequence analysis of tryptic peptides of this material revealed in addition to transthyretin sequences, also amino acid sequence corresponding to an N-terminal fragment of apolipoprotein A-IV. In immunohistochemistry, an antiserum to a synthetic apolipoprotein A-IV peptide labeled amyloid specifically. This peptide formed spontaneously amyloid-like fibrils in vitro and enhanced fibril formation from wild-type transthyretin. We conclude that several apolipoproteins, including apolipoprotein A-IV, may be important minor amyloid constituents, promoting fibril formation.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
amyloid transthyretin apolipoprotein A-IV fibrillogenesis chaperones
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 285,
Issue: 4,
Pages: 903-908
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institute of Molecular Immunology (IMI)